A Hemoglobin with an Optical Function

Hemoglobins are best known as oxygen transport pro-teins. Here we describe a hemoglobin from the parasitic nematode Mermis nigrescens (Mn-GLB-E) that has an optical, light shadowing function. The protein accumu-lates to high concentration as intracellular crystals in the ocellus of mature phototactic adult females while also being expressed at low concentration in other tis-sues. It differs in sequence and expression pattern from Mn-GLB-B, a second Mermis globin. It retains the struc-ture and oxygen-binding and light-absorbing properties typical of nematode hemoglobins. As such, recruitment to a shadowing role in the eye appears to have occurred by changes in expression without modification of bio-chemistry. Both globins are coded by genes interrupted by two introns at the conserved positions B12.2 and G7.0, which is in agreement with the 3exon/2intron pat-tern model of globin gene evolution.